REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.DING,K.DAS,Y.HSIOU,S.G.SARAFIANOS,A.D.CLARK JR., REMARK 1 AUTH 2 A.JACOBO-MOLINA,C.TANTILLO,S.H.HUGHES,E.ARNOLD REMARK 1 TITL STRUCTURE AND FUNCTIONAL IMPLICATIONS OF THE REMARK 1 TITL 2 POLYMERASE ACTIVE SITE REGION IN A COMPLEX OF REMARK 1 TITL 3 HIV-1 RT WITH A DOUBLE-STRANDED DNA REMARK 1 TITL 4 TEMPLATE-PRIMER AND AN ANTIBODY FAB FRAGMENT AT REMARK 1 TITL 5 2.8 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 284 1095 1998 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1998.2208 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.G.SARAFIANOS,K.DAS,J.DING,P.L.BOYER,S.H.HUGHES, REMARK 1 AUTH 2 E.ARNOLD REMARK 1 TITL TOUCHING THE HEART OF HIV-1 DRUG RESISTANCE: THE REMARK 1 TITL 2 FINGERS CLOSE DOWN ON THE DNTP AT THE POLYMERASE REMARK 1 TITL 3 ACTIVE SITE REMARK 1 REF CHEM.BIOL. V. 6 R137 1999 REMARK 1 REFN ISSN 1074-5521 REMARK 1 DOI 10.1016/S1074-5521(99)80071-4 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5 REMARK 3 NUMBER OF REFLECTIONS : 39033 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.262 REMARK 3 FREE R VALUE : 0.338 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1700 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 10967 REMARK 3 NUCLEIC ACID ATOMS : 753 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.68 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1J5O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-02. REMARK 100 THE RCSB ID CODE IS RCSB001643. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-SEP-96; 10-JUN-97 REMARK 200 TEMPERATURE (KELVIN) : 277; 105 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 10 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : CHESS; NSLS REMARK 200 BEAMLINE : F1; X25 REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.918; 1.1 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : FUJI; MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42062 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4 REMARK 200 DATA REDUNDANCY : 5.910 REMARK 200 R MERGE (I) : 0.11800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : 0.40000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % SATURATED AMMONIUM SULFATE, REMARK 280 100 MM CACODYLATE PH 5.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -Y,-X,-Z+1/3 REMARK 290 5555 -X+Y,Y,-Z+2/3 REMARK 290 6555 X,X-Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.94000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.97000 REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 73.97000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 147.94000 REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, A, B, L, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 13 CG CD CE NZ REMARK 470 GLU A 28 CG CD OE1 OE2 REMARK 470 LYS A 30 CG CD CE NZ REMARK 470 LYS A 32 CG CD CE NZ REMARK 470 GLU A 36 CG CD OE1 OE2 REMARK 470 GLU A 40 CG CD OE1 OE2 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LYS A 66 CG CD CE NZ REMARK 470 ASP A 67 CG OD1 OD2 REMARK 470 SER A 68 OG REMARK 470 THR A 69 OG1 CG2 REMARK 470 LYS A 70 CG CD CE NZ REMARK 470 TRP A 71 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 71 CZ3 CH2 REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 73 CG CD CE NZ REMARK 470 ASN A 136 CG OD1 ND2 REMARK 470 GLU A 138 CG CD OE1 OE2 REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 203 CG CD OE1 OE2 REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 222 CG CD OE1 NE2 REMARK 470 LYS A 223 CG CD CE NZ REMARK 470 LYS A 238 CG CD CE NZ REMARK 470 GLN A 242 CG CD OE1 NE2 REMARK 470 ILE A 244 CG1 CG2 CD1 REMARK 470 VAL A 245 CG1 CG2 REMARK 470 PRO A 247 CG CD REMARK 470 GLU A 248 CG CD OE1 OE2 REMARK 470 LYS A 249 CG CD CE NZ REMARK 470 ASP A 250 CG OD1 OD2 REMARK 470 TRP A 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 252 CZ3 CH2 REMARK 470 THR A 253 OG1 CG2 REMARK 470 LYS A 275 CG CD CE NZ REMARK 470 GLN A 278 CG CD OE1 NE2 REMARK 470 LYS A 281 CG CD CE NZ REMARK 470 LEU A 282 CG CD1 CD2 REMARK 470 LEU A 283 CG CD1 CD2 REMARK 470 ARG A 284 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 289 CG CD1 CD2 REMARK 470 THR A 290 OG1 CG2 REMARK 470 VAL A 292 CG1 CG2 REMARK 470 ILE A 293 CG1 CG2 CD1 REMARK 470 PRO A 294 CG CD REMARK 470 LEU A 295 CG CD1 CD2 REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 GLU A 298 CG CD OE1 OE2 REMARK 470 GLU A 300 CG CD OE1 OE2 REMARK 470 GLU A 302 CG CD OE1 OE2 REMARK 470 GLU A 305 CG CD OE1 OE2 REMARK 470 ASN A 306 CG OD1 ND2 REMARK 470 ILE A 309 CG1 CG2 CD1 REMARK 470 LYS A 311 CG CD CE NZ REMARK 470 GLU A 312 CG CD OE1 OE2 REMARK 470 LYS A 331 CG CD CE NZ REMARK 470 ARG A 448 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 449 CG CD OE1 OE2 REMARK 470 GLN A 524 CG CD OE1 NE2 REMARK 470 LYS A 530 CG CD CE NZ REMARK 470 LYS A 540 CG CD CE NZ REMARK 470 GLU A 546 CG CD OE1 OE2 REMARK 470 GLN A 547 CG CD OE1 NE2 REMARK 470 LYS A 550 CG CD CE NZ REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 558 CG CD CE NZ REMARK 470 LYS B 13 CG CD CE NZ REMARK 470 VAL B 90 CG1 CG2 REMARK 470 GLN B 91 CG CD OE1 NE2 REMARK 470 LYS B 173 CG CD CE NZ REMARK 470 THR B 240 OG1 CG2 REMARK 470 VAL B 241 CG1 CG2 REMARK 470 GLN B 242 CG CD OE1 NE2 REMARK 470 PRO B 243 CG CD REMARK 470 ILE B 244 CG1 CG2 CD1 REMARK 470 VAL B 245 CG1 CG2 REMARK 470 LEU B 246 CG CD1 CD2 REMARK 470 PRO B 247 CG CD REMARK 470 GLU B 248 CG CD OE1 OE2 REMARK 470 LYS B 249 CG CD CE NZ REMARK 470 ASP B 250 CG OD1 OD2 REMARK 470 SER B 251 OG REMARK 470 TRP B 252 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 252 CZ3 CH2 REMARK 470 SER B 268 OG REMARK 470 LYS B 275 CG CD CE NZ REMARK 470 VAL B 276 CG1 CG2 REMARK 470 ARG B 277 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 278 CG CD OE1 NE2 REMARK 470 LYS B 281 CG CD CE NZ REMARK 470 LEU B 282 CG CD1 CD2 REMARK 470 ARG B 284 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 291 CG CD OE1 OE2 REMARK 470 VAL B 292 CG1 CG2 REMARK 470 ILE B 293 CG1 CG2 CD1 REMARK 470 GLU B 297 CG CD OE1 OE2 REMARK 470 GLU B 298 CG CD OE1 OE2 REMARK 470 GLU B 300 CG CD OE1 OE2 REMARK 470 GLU B 305 CG CD OE1 OE2 REMARK 470 GLU B 308 CG CD OE1 OE2 REMARK 470 ILE B 309 CG1 CG2 CD1 REMARK 470 LEU B 310 CG CD1 CD2 REMARK 470 LYS B 311 CG CD CE NZ REMARK 470 GLU B 312 CG CD OE1 OE2 REMARK 470 PRO B 313 CG CD REMARK 470 VAL B 314 CG1 CG2 REMARK 470 HIS B 315 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 424 CG CD CE NZ REMARK 470 GLN B 428 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO B 243 N - CA - CB ANGL. DEV. = 7.6 DEGREES REMARK 500 PRO B 247 N - CA - CB ANGL. DEV. = 8.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 4 30.86 -91.77 REMARK 500 MET A 16 172.30 -57.41 REMARK 500 GLU A 53 -6.53 -155.83 REMARK 500 ILE A 63 95.95 -177.20 REMARK 500 LYS A 66 87.70 -25.16 REMARK 500 LYS A 73 76.38 -163.05 REMARK 500 ASP A 76 75.55 -112.93 REMARK 500 PHE A 77 29.84 -68.57 REMARK 500 GLN A 91 112.15 170.61 REMARK 500 LEU A 92 44.55 -97.76 REMARK 500 HIS A 96 129.65 179.52 REMARK 500 LYS A 101 -153.54 -87.13 REMARK 500 ASP A 113 10.80 56.13 REMARK 500 ALA A 114 -72.36 -14.43 REMARK 500 PHE A 116 -1.93 -56.44 REMARK 500 THR A 128 40.15 -66.11 REMARK 500 ASN A 136 -80.17 3.67 REMARK 500 ASN A 137 -82.58 -23.32 REMARK 500 GLN A 151 -8.25 -52.07 REMARK 500 LYS A 154 -38.11 -35.48 REMARK 500 SER A 156 -61.33 -18.65 REMARK 500 PRO A 157 -71.42 -33.13 REMARK 500 GLN A 161 -73.82 -56.72 REMARK 500 SER A 163 -70.55 -61.75 REMARK 500 MET A 164 -33.59 -35.80 REMARK 500 ASP A 177 -37.14 -162.02 REMARK 500 ILE A 184 -101.53 56.18 REMARK 500 SER A 191 150.28 179.74 REMARK 500 ILE A 195 -37.07 -23.30 REMARK 500 THR A 216 71.97 -114.16 REMARK 500 ASP A 218 -2.50 -58.53 REMARK 500 LYS A 219 48.34 -80.68 REMARK 500 LYS A 223 85.93 -54.27 REMARK 500 GLU A 224 -71.23 -35.26 REMARK 500 MET A 230 21.93 47.59 REMARK 500 PRO A 236 -1.50 -55.92 REMARK 500 ASP A 237 -22.15 -156.97 REMARK 500 VAL A 241 76.07 -117.86 REMARK 500 PRO A 243 19.51 -58.06 REMARK 500 ILE A 244 56.35 -68.75 REMARK 500 SER A 251 75.36 -6.12 REMARK 500 TRP A 252 -71.42 -173.36 REMARK 500 ARG A 284 -146.75 -75.61 REMARK 500 LEU A 295 12.10 -61.65 REMARK 500 VAL A 314 -166.96 -100.94 REMARK 500 HIS A 315 160.43 170.16 REMARK 500 LYS A 323 -152.63 -89.94 REMARK 500 GLN A 332 -68.99 -93.33 REMARK 500 GLN A 340 119.54 -170.64 REMARK 500 PRO A 345 -101.39 2.25 REMARK 500 LYS A 350 148.52 179.94 REMARK 500 TYR A 354 140.99 -173.33 REMARK 500 ALA A 355 23.88 -155.35 REMARK 500 ARG A 358 -107.60 -62.13 REMARK 500 THR A 376 -81.85 -47.82 REMARK 500 ILE A 393 134.38 174.22 REMARK 500 THR A 397 -75.87 -69.24 REMARK 500 TYR A 405 102.49 -58.11 REMARK 500 GLN A 407 120.08 -175.81 REMARK 500 GLU A 413 127.30 -35.82 REMARK 500 THR A 419 -69.60 -152.71 REMARK 500 PRO A 421 78.40 -63.59 REMARK 500 LEU A 422 128.23 -34.66 REMARK 500 TRP A 426 -88.40 -81.82 REMARK 500 LEU A 429 153.74 -48.54 REMARK 500 PRO A 433 99.27 -53.27 REMARK 500 PHE A 440 170.79 -57.25 REMARK 500 ASP A 443 162.27 179.88 REMARK 500 ALA A 445 170.13 163.66 REMARK 500 LYS A 451 -1.52 71.53 REMARK 500 ALA A 455 108.21 -160.42 REMARK 500 LYS A 461 42.39 -75.10 REMARK 500 LYS A 465 147.90 160.20 REMARK 500 ASN A 471 64.48 71.40 REMARK 500 LEU A 484 -79.36 -55.74 REMARK 500 ALA A 485 -39.56 -35.31 REMARK 500 ASP A 488 44.78 -87.34 REMARK 500 SER A 489 -140.75 -117.81 REMARK 500 VAL A 493 130.36 171.93 REMARK 500 TYR A 501 -71.70 -36.59 REMARK 500 GLN A 509 65.45 74.14 REMARK 500 SER A 513 135.15 166.79 REMARK 500 LYS A 528 159.16 -38.80 REMARK 500 ALA A 538 -81.69 -100.42 REMARK 500 HIS A 539 5.35 -57.74 REMARK 500 ILE A 556 154.85 179.43 REMARK 500 ILE B 2 151.28 -46.86 REMARK 500 GLU B 6 -174.93 -63.25 REMARK 500 LEU B 12 167.99 -34.25 REMARK 500 ASP B 17 49.47 -64.84 REMARK 500 LYS B 20 33.68 -166.76 REMARK 500 GLU B 36 -71.36 -38.39 REMARK 500 GLU B 53 -29.98 -35.20 REMARK 500 ASN B 57 150.90 177.00 REMARK 500 ILE B 63 85.19 -175.25 REMARK 500 LYS B 64 91.30 -53.75 REMARK 500 ASP B 67 173.26 179.91 REMARK 500 LYS B 70 -173.92 -60.21 REMARK 500 TRP B 71 -179.02 -66.02 REMARK 500 ASP B 76 72.37 -68.74 REMARK 500 GLN B 85 177.87 -42.77 REMARK 500 VAL B 90 -75.21 -70.83 REMARK 500 ASP B 113 -37.39 -26.87 REMARK 500 PRO B 119 -150.99 -73.75 REMARK 500 LEU B 120 133.19 -171.85 REMARK 500 ASP B 121 130.28 -35.60 REMARK 500 PHE B 124 -14.02 -45.25 REMARK 500 LYS B 126 -14.87 -42.67 REMARK 500 TYR B 127 30.37 -89.75 REMARK 500 ASN B 136 9.81 49.27 REMARK 500 VAL B 148 -143.72 -101.10 REMARK 500 TRP B 153 124.99 173.42 REMARK 500 SER B 156 -70.01 -53.99 REMARK 500 PHE B 160 -13.38 -45.27 REMARK 500 ASN B 175 94.92 166.00 REMARK 500 ILE B 184 -119.26 57.85 REMARK 500 LEU B 214 48.64 34.22 REMARK 500 ASP B 218 -175.59 -67.08 REMARK 500 PRO B 225 -103.27 -62.15 REMARK 500 PHE B 227 78.34 -27.31 REMARK 500 TYR B 232 -31.67 -39.80 REMARK 500 ASP B 237 -53.48 -9.61 REMARK 500 GLN B 242 76.44 -50.01 REMARK 500 VAL B 245 106.53 -169.12 REMARK 500 PRO B 247 151.77 159.91 REMARK 500 GLU B 248 67.10 -165.66 REMARK 500 SER B 251 70.10 -179.84 REMARK 500 ILE B 270 -65.46 -93.17 REMARK 500 THR B 286 54.36 -37.85 REMARK 500 GLU B 291 -27.52 62.25 REMARK 500 ILE B 293 63.34 -109.38 REMARK 500 PRO B 294 47.24 -62.17 REMARK 500 LEU B 295 120.14 -39.74 REMARK 500 GLU B 312 -167.52 -117.07 REMARK 500 VAL B 317 107.31 -45.30 REMARK 500 LYS B 331 23.42 -74.52 REMARK 500 GLN B 332 91.11 -42.04 REMARK 500 PHE B 346 7.22 57.46 REMARK 500 ALA B 355 -159.94 -99.36 REMARK 500 ARG B 358 35.77 34.91 REMARK 500 ALA B 360 1.09 -57.10 REMARK 500 ASN B 363 97.21 -167.74 REMARK 500 ASP B 364 -67.89 -26.00 REMARK 500 ILE B 382 -111.17 -84.59 REMARK 500 TRP B 383 -1.50 -58.11 REMARK 500 LYS B 385 -174.23 -62.30 REMARK 500 LYS B 390 97.53 -69.82 REMARK 500 LYS B 395 -87.76 -38.45 REMARK 500 GLU B 396 -48.40 -22.23 REMARK 500 THR B 397 -74.81 -60.15 REMARK 500 GLU B 399 -79.99 -51.10 REMARK 500 THR B 400 -3.13 -43.31 REMARK 500 GLU B 404 -11.02 -49.48 REMARK 500 GLN B 407 12.36 -161.13 REMARK 500 LYS B 424 -3.83 -59.20 REMARK 500 LEU B 425 29.32 -74.24 REMARK 500 TRP B 426 -21.29 56.36 REMARK 500 LEU B 429 89.03 -56.43 REMARK 500 ALA L 13 -169.81 -110.67 REMARK 500 GLN L 27 161.17 170.93 REMARK 500 TYR L 32 57.47 -98.36 REMARK 500 THR L 43 156.55 -45.30 REMARK 500 THR L 51 -3.98 70.70 REMARK 500 SER L 52 -7.13 -166.89 REMARK 500 SER L 76 -70.19 -70.31 REMARK 500 PRO L 80 -3.14 -27.77 REMARK 500 PHE L 83 82.66 -67.68 REMARK 500 SER L 92 -95.30 -93.07 REMARK 500 PHE L 94 -31.88 -34.85 REMARK 500 ASP L 110 171.29 -40.66 REMARK 500 ALA L 111 147.43 -175.87 REMARK 500 ASN L 138 87.03 41.05 REMARK 500 TYR L 140 -70.82 -73.77 REMARK 500 ASP L 143 112.28 -35.46 REMARK 500 ASP L 151 99.30 -19.75 REMARK 500 SER L 153 45.22 16.63 REMARK 500 ALA L 156 162.77 -43.18 REMARK 500 ASP L 167 108.93 -53.38 REMARK 500 SER L 168 0.38 -55.37 REMARK 500 LYS L 169 -78.70 -92.51 REMARK 500 SER L 171 11.20 49.51 REMARK 500 THR L 172 -159.97 -84.04 REMARK 500 SER L 176 112.82 -165.48 REMARK 500 ALA L 188 -71.50 -57.58 REMARK 500 ASN L 190 -81.82 -93.16 REMARK 500 LYS L 199 44.35 -67.10 REMARK 500 THR L 200 -82.52 -83.32 REMARK 500 SER L 201 36.27 -144.88 REMARK 500 ALA L 211 94.44 -173.75 REMARK 500 PRO H 14 172.17 -52.77 REMARK 500 LEU H 29 31.41 -90.00 REMARK 500 SER H 32 -52.04 -26.97 REMARK 500 ALA H 51 -177.00 -175.86 REMARK 500 ASP H 57 13.31 88.36 REMARK 500 LYS H 66 -57.77 -24.26 REMARK 500 LYS H 73 105.38 -170.43 REMARK 500 ASP H 74 95.60 -69.26 REMARK 500 SER H 76 -30.03 -32.10 REMARK 500 THR H 86 48.74 35.75 REMARK 500 THR H 89 -78.82 -17.16 REMARK 500 ALA H 90 -53.82 -24.79 REMARK 500 ALA H 93 -176.65 -174.07 REMARK 500 VAL H 105 -16.98 -43.29 REMARK 500 MET H 110 74.75 -100.92 REMARK 500 TRP H 113 -144.86 -115.35 REMARK 500 GLN H 115 111.41 -18.33 REMARK 500 SER H 122 132.72 -178.12 REMARK 500 ALA H 124 146.41 -34.73 REMARK 500 THR H 126 106.47 -22.86 REMARK 500 SER H 138 -69.53 -29.74 REMARK 500 ALA H 140 -176.75 -65.69 REMARK 500 GLN H 141 109.10 -59.68 REMARK 500 THR H 142 -81.33 -106.32 REMARK 500 PHE H 156 -64.90 -102.00 REMARK 500 VAL H 160 112.31 -169.66 REMARK 500 SER H 170 -17.90 -149.69 REMARK 500 LEU H 180 63.77 -53.36 REMARK 500 SER H 200 -95.18 -88.69 REMARK 500 SER H 213 48.03 28.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 DC P 836 0.06 SIDE_CHAIN REMARK 500 TYR A 144 0.09 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QE1 RELATED DB: PDB REMARK 900 UNLIGANDED MET184ILE HIV-1 REVERSE TRANSCRIPTASE REMARK 900 RELATED ID: 2HMI RELATED DB: PDB REMARK 900 WILD-TYPE HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH A REMARK 900 DOUBLE STRANDED DNA TEMPLATE-PRIMER